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American Journal of Pathology, Vol 138, 619-628, Copyright © 1991 by American Society for Investigative Pathology

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S-100 protein antibodies do not label normal salivary gland myoepithelium. Histogenetic implications for salivary gland tumors

I Dardick, M Stratis, WR Parks, FG DeNardi and HJ Kahn
Department of Pathology, Toronto General Hospital, Ontario, Canada.

Neoplastically modified myoepithelial cells have a key role in developing the histologic characteristics of some salivary gland tumors. S-100 protein expressed in certain of these tumors is suggested to support this role, as the principal component in the human salivary gland reported to be S-100 protein-positive is myoepithelium. Confirmation of such an important aspect is required. Immunoperoxidase staining of parotid salivary gland shows considerably different patterns obtained with antibodies to S-100 protein, neuron-specific enolase, and neurofilaments compared with those for muscle-specific actin and cytokeratin 14; many more cells and their processes associated with acini and ducts are evident with the latter two antibodies. Double immunofluorescent staining with antibodies to either S-100 protein or neuron-specific enolase combined with muscle-specific actin does not reveal colocalization of these antigens in myoepithelial cells. The former localize only to nerve fibers adjacent to, but separate from, acini, and the latter only to myoepithelial cells. It is apparent that S-100 protein staining of the rich network of unmyelinated nerves in the interstitial tissues, evident ultrastructurally, has been misinterpreted as myoepithelium. This result has important implications for histogenetic classifications of salivary gland tumors.

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